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Q0WLB5

- CLAH2_ARATH

UniProt

Q0WLB5 - CLAH2_ARATH

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Protein

Clathrin heavy chain 2

Gene

CHC2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Clathrin is the major protein of the polyhedral coat of coated pits and vesicles (By similarity). Mediates endocytosis and is required for a correct polar distribution of PIN auxin transporters.By similarity1 Publication

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. endocytosis Source: TAIR
  2. intracellular protein transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin heavy chain 2
Gene namesi
Name:CHC2
Synonyms:CHC1
Ordered Locus Names:At3g08530
ORF Names:F17O14.1, T8G24.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G08530.

Subcellular locationi

Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Membranecoated pit By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: Cytoplasmic face of coated pits and vesicles.By similarity

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. clathrin coat of coated pit Source: InterPro
  3. clathrin coat of trans-Golgi network vesicle Source: InterPro
  4. cytosol Source: TAIR
  5. Golgi apparatus Source: TAIR
  6. membrane Source: TAIR
  7. plasma membrane Source: TAIR
  8. plasmodesma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

Defective in bulk endocytosis as well as in internalization of prominent plasma membrane proteins. Defects in constitutive endocytic recycling of PIN auxin transporters and their polar distribution in embryos and roots leading to altered auxin distribution patterns and associated auxin transport-related phenotypes. Defective in embryonic and postembryonic development.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 17031702Clathrin heavy chain 2PRO_0000413950Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ0WLB5.
PRIDEiQ0WLB5.

Expressioni

Gene expression databases

ExpressionAtlasiQ0WLB5. baseline.
GenevestigatoriQ0WLB5.

Interactioni

Subunit structurei

Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat (By similarity). Interacts with CLC2 and TPLATE.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TPLATEF4J8D32EBI-4412194,EBI-4412119

Protein-protein interaction databases

BioGridi5336. 47 interactions.
DIPiDIP-59590N.
IntActiQ0WLB5. 51 interactions.
STRINGi3702.AT3G08530.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ0WLB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati551 – 697147CHCR 1Add
BLAST
Repeati700 – 842143CHCR 2Add
BLAST
Repeati847 – 986140CHCR 3Add
BLAST
Repeati993 – 1138146CHCR 4Add
BLAST
Repeati1142 – 1283142CHCR 5Add
BLAST
Repeati1288 – 1434147CHCR 6Add
BLAST
Repeati1437 – 1580144CHCR 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 492491Globular terminal domainBy similarityAdd
BLAST
Regioni25 – 6743WD40-like repeat 1Add
BLAST
Regioni68 – 11346WD40-like repeat 2Add
BLAST
Regioni114 – 15542WD40-like repeat 3Add
BLAST
Regioni156 – 20550WD40-like repeat 4Add
BLAST
Regioni206 – 27065WD40-like repeat 5Add
BLAST
Regioni271 – 31444WD40-like repeat 6Add
BLAST
Regioni315 – 34329WD40-like repeat 7Add
BLAST
Regioni462 – 47817Binding site for the uncoating ATPase, involved in lattice disassemblyBy similarityAdd
BLAST
Regioni493 – 53644Flexible linkerBy similarityAdd
BLAST
Regioni537 – 17031167Heavy chain armBy similarityAdd
BLAST
Regioni537 – 648112Distal segmentBy similarityAdd
BLAST
Regioni653 – 17031051Proximal segmentBy similarityAdd
BLAST
Regioni1227 – 1536310Involved in binding clathrin light chainBy similarityAdd
BLAST
Regioni1564 – 1703140TrimerizationBy similarityAdd
BLAST

Domaini

The C-terminal third of the heavy chains forms the hub of the triskelion. This region contains the trimerization domain and the light-chain binding domain involved in the assembly of the clathrin lattice.
The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It consitutes a major protein-protein interaction node (By similarity).By similarity

Sequence similaritiesi

Belongs to the clathrin heavy chain family.Curated
Contains 7 CHCR (clathrin heavy-chain) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG314149.
HOGENOMiHOG000188877.
InParanoidiQ0WLB5.
KOiK04646.
OMAiWKWFSEK.
PhylomeDBiQ0WLB5.

Family and domain databases

Gene3Di1.25.40.10. 3 hits.
2.130.10.110. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000547. Clathrin_H-chain/VPS_repeat.
IPR016025. Clathrin_H-chain_link/propller.
IPR015348. Clathrin_H-chain_linker_core.
IPR001473. Clathrin_H-chain_propeller_N.
IPR022365. Clathrin_H-chain_propeller_rpt.
IPR016341. Clathrin_heavy_chain.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PfamiPF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 2 hits.
[Graphical view]
PIRSFiPIRSF002290. Clathrin_H_chain. 1 hit.
SMARTiSM00299. CLH. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 5 hits.
SSF50989. SSF50989. 1 hit.
PROSITEiPS50236. CHCR. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0WLB5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAANAPITM KEVLTLPSIG INQQFITFTN VTMESDKYIC VRETSPQNSV
60 70 80 90 100
VIIDMNMPMQ PLRRPITADS ALMNPNSKIL ALKAQVPGTT QDHLQIFNIE
110 120 130 140 150
AKAKLKSHQM PEQVVFWKWI TPKMLGLVTQ NSVYHWSIEG DSEPVKMFDR
160 170 180 190 200
TANLANNQII NYKCSPNEKW LVLIGIAPGS PERQQLVKGN MQLFSVDQQR
210 220 230 240 250
SQALEAHAAS FAQFKVPGNE NPSILISFAS KSFNAGQITS KLHVIELGAQ
260 270 280 290 300
PGKPSFTKKQ ADLFFPPDFA DDFPVAMQVS HKFNLIYVIT KLGLLFVYDL
310 320 330 340 350
ETASAIYRNR ISPDPIFLTS EASSVGGFYA INRRGQVLLA TVNEATIIPF
360 370 380 390 400
ISGQLNNLEL AVNLAKRGNL PGAENLVVQR FQELFAQTKY KEAAELAAES
410 420 430 440 450
PQGILRTPDT VAKFQSVPVQ AGQTPPLLQY FGTLLTRGKL NSYESLELSR
460 470 480 490 500
LVVNQNKKNL LENWLAEDKL ECSEELGDLV KTVDNDLALK IYIKARATPK
510 520 530 540 550
VVAAFAERRE FDKILIYSKQ VGYTPDYLFL LQTILRTDPQ GAVNFALMMS
560 570 580 590 600
QMEGGSPVDY NTITDLFLQR NLIREATSFL LDVLKPNLPE HAFLQTKVLE
610 620 630 640 650
INLVTFPNVA DAVLANGMFT HYDRPRIAQL CEKAGLYIQS LKHYSELPDI
660 670 680 690 700
KRVIVNTHAI EPQALVEFFG TLSSEWAMEC MKDLLLVNLR GNLQIIVQAC
710 720 730 740 750
KEYCEQLGVD ACIKLFEQFK SYEGLYFFLG SYLSMSEDPE IHFKYIEAAA
760 770 780 790 800
KTGQIKEVER VTRESNFYDA EKTKNFLMEA KLPDARPLIN VCDRFSFVPD
810 820 830 840 850
LTHYLYTNNM LRYIEGYVQK VNPGNAPLVV GQLLDDECPE DFIKGLILSV
860 870 880 890 900
RSLLPVEPLV EECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDS
910 920 930 940 950
NNNPEHFLTT NPYYDSKVVG KYCEKRDPTL AVVAYRRGQC DEELINVTNK
960 970 980 990 1000
NSLFKLQARY VVERMDGDLW DKVLDENNDY RRQLIDQVVS TALPESKSPE
1010 1020 1030 1040 1050
QVSAAVKAFM TADLPHELIE LLEKIVLQNS AFSGNFNLQN LLILTAIKAD
1060 1070 1080 1090 1100
PSRVMDYINR LDNFDGPAVG EVAVEAQLYE EAFAIFKKFN LNVQAVNVLL
1110 1120 1130 1140 1150
DNVRSIERAV EFAFRVEEDS VWSQVAKAQL REGLVSDAIE SFIRADDATH
1160 1170 1180 1190 1200
FLEVIRVSED TDVYDDLVKY LLMVRQKVKE PKVDSELIYA YAKIDRLGEI
1210 1220 1230 1240 1250
EEFILMPNVA NLQHVGDRLY DEALYEAAKI IYAFISNWGK LAVTLVKLQQ
1260 1270 1280 1290 1300
FQGAVDAARK ANSAKTWKEV CFACVDAEEF RLAQICGLNI IIQVDDLEEV
1310 1320 1330 1340 1350
SEYYQNRGCF NELISLMESG LGLERAHMGI FTELGVLYAR YRYEKLMEHI
1360 1370 1380 1390 1400
KLFSTRLNIP KLIRACDEQQ HWQELTYLYI QYDEFDNAAT TVMNHSPEAW
1410 1420 1430 1440 1450
EHMQFKDIVA KVANVELYYK AVHFYLQEHP DIINDLLNVL ALRLDHTRVV
1460 1470 1480 1490 1500
DIMRKAGHLR LIKPYMIAVQ SNNVSAVNEA LNEIYVEEED YDRLRESIDL
1510 1520 1530 1540 1550
HDSFDQIGLA QKIEKHELVE MRRVAAYIYK KAGRWKQSIA LSKKDNMYKD
1560 1570 1580 1590 1600
CMETASQSGE HELAEQLLVY FIEQGKKECF ATCLFVCYDL IRPDVALELA
1610 1620 1630 1640 1650
WINNMMDFAF PYLLQFIREY SGKVDELIKD KLEAQKEVKA KEQEEKDVIS
1660 1670 1680 1690 1700
QQNMYAQMLP LALPAPPMPG MGGGGGYGPP PQMGGMPGMP PMPPYGMPPM

GGY
Length:1,703
Mass (Da):193,271
Last modified:September 5, 2006 - v1
Checksum:i6A91D665A841F504
GO

Sequence cautioni

The sequence AAG50828.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG51341.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAM19776.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012562 Genomic DNA. Translation: AAG51341.1. Sequence problems.
AC074395 Genomic DNA. Translation: AAG50828.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74644.1.
AK230290 mRNA. Translation: BAF02092.1.
AY094397 mRNA. Translation: AAM19776.1. Different initiation.
AY125528 mRNA. Translation: AAM78038.1.
RefSeqiNP_187466.4. NM_111688.6.
UniGeneiAt.17332.
At.26828.

Genome annotation databases

EnsemblPlantsiAT3G08530.1; AT3G08530.1; AT3G08530.
GeneIDi820001.
KEGGiath:AT3G08530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC012562 Genomic DNA. Translation: AAG51341.1 . Sequence problems.
AC074395 Genomic DNA. Translation: AAG50828.1 . Sequence problems.
CP002686 Genomic DNA. Translation: AEE74644.1 .
AK230290 mRNA. Translation: BAF02092.1 .
AY094397 mRNA. Translation: AAM19776.1 . Different initiation.
AY125528 mRNA. Translation: AAM78038.1 .
RefSeqi NP_187466.4. NM_111688.6.
UniGenei At.17332.
At.26828.

3D structure databases

ProteinModelPortali Q0WLB5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 5336. 47 interactions.
DIPi DIP-59590N.
IntActi Q0WLB5. 51 interactions.
STRINGi 3702.AT3G08530.1-P.

Proteomic databases

PaxDbi Q0WLB5.
PRIDEi Q0WLB5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G08530.1 ; AT3G08530.1 ; AT3G08530 .
GeneIDi 820001.
KEGGi ath:AT3G08530.

Organism-specific databases

TAIRi AT3G08530.

Phylogenomic databases

eggNOGi NOG314149.
HOGENOMi HOG000188877.
InParanoidi Q0WLB5.
KOi K04646.
OMAi WKWFSEK.
PhylomeDBi Q0WLB5.

Miscellaneous databases

PROi Q0WLB5.

Gene expression databases

ExpressionAtlasi Q0WLB5. baseline.
Genevestigatori Q0WLB5.

Family and domain databases

Gene3Di 1.25.40.10. 3 hits.
2.130.10.110. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR000547. Clathrin_H-chain/VPS_repeat.
IPR016025. Clathrin_H-chain_link/propller.
IPR015348. Clathrin_H-chain_linker_core.
IPR001473. Clathrin_H-chain_propeller_N.
IPR022365. Clathrin_H-chain_propeller_rpt.
IPR016341. Clathrin_heavy_chain.
IPR011990. TPR-like_helical_dom.
[Graphical view ]
Pfami PF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 2 hits.
[Graphical view ]
PIRSFi PIRSF002290. Clathrin_H_chain. 1 hit.
SMARTi SM00299. CLH. 7 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 5 hits.
SSF50989. SSF50989. 1 hit.
PROSITEi PS50236. CHCR. 7 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1703.
    Strain: cv. Columbia.
  5. "Clathrin mediates endocytosis and polar distribution of PIN auxin transporters in Arabidopsis."
    Kitakura S., Vanneste S., Robert S., Loefke C., Teichmann T., Tanaka H., Friml J.
    Plant Cell 23:1920-1931(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Adaptin-like protein TPLATE and clathrin recruitment during plant somatic cytokinesis occurs via two distinct pathways."
    Van Damme D., Gadeyne A., Vanstraelen M., Inze D., Van Montagu M.C., De Jaeger G., Russinova E., Geelen D.
    Proc. Natl. Acad. Sci. U.S.A. 108:615-620(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLC2 AND TPLATE.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCLAH2_ARATH
AccessioniPrimary (citable) accession number: Q0WLB5
Secondary accession number(s): Q8L3R8, Q9C6U0, Q9CA00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2011
Last sequence update: September 5, 2006
Last modified: October 29, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

Was assigned to CHC1 in PubMed:21187379.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3